ID S5XRU7_PARAH Unreviewed; 282 AA.
AC S5XRU7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Release factor glutamine methyltransferase {ECO:0000256|HAMAP-Rule:MF_02126};
DE Short=RF MTase {ECO:0000256|HAMAP-Rule:MF_02126};
DE EC=2.1.1.297 {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=N5-glutamine methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-(glutamine-N5) MTase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
DE AltName: Full=Protein-glutamine N-methyltransferase PrmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN Name=prmC {ECO:0000256|HAMAP-Rule:MF_02126};
GN ORFNames=JCM7686_0728 {ECO:0000313|EMBL:AGT07837.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07837.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT07837.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07837.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
CC -!- FUNCTION: Methylates the class 1 translation termination release
CC factors RF1/PrfA and RF2/PrfB on the glutamine residue of the
CC universally conserved GGQ motif. {ECO:0000256|HAMAP-Rule:MF_02126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000256|ARBA:ARBA00000932, ECO:0000256|HAMAP-
CC Rule:MF_02126};
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. PrmC subfamily. {ECO:0000256|HAMAP-Rule:MF_02126}.
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DR EMBL; CP006650; AGT07837.1; -; Genomic_DNA.
DR RefSeq; WP_020949476.1; NC_022041.1.
DR AlphaFoldDB; S5XRU7; -.
DR STRING; 1367847.JCM7686_0728; -.
DR KEGG; pami:JCM7686_0728; -.
DR PATRIC; fig|1367847.3.peg.679; -.
DR eggNOG; COG2890; Bacteria.
DR HOGENOM; CLU_018398_3_1_5; -.
DR OrthoDB; 9800643at2; -.
DR Proteomes; UP000015480; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036009; F:protein-glutamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_02126; RF_methyltr_PrmC; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR NCBIfam; TIGR00536; hemK_fam; 1.
DR NCBIfam; TIGR03534; RF_mod_PrmC; 1.
DR PANTHER; PTHR18895; HEMK METHYLTRANSFERASE; 1.
DR PANTHER; PTHR18895:SF74; MTRF1L RELEASE FACTOR GLUTAMINE METHYLTRANSFERASE; 1.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02126}; Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02126};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02126}.
FT DOMAIN 10..80
FT /note="Release factor glutamine methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17827"
FT DOMAIN 102..193
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
FT BINDING 121..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 189..192
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
FT BINDING 189
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02126"
SQ SEQUENCE 282 AA; 30053 MW; 86FB4D6ED0B4CEB7 CRC64;
MTASAQSGAE LLRAAALRLT DAGVEGAERD AQILFLHALG LPRHRLNEAL TTPPEPEAAA
RFEAAIAART ARQPVSQITG RRAFWMHDFE VTRDTLDPRA ETELLVETGL EAPFLRVLDM
GTGTGAILLS LLAERPGATG IGSDISDAAL AVARRNAARI GTAVAGRAEF ILSDWYEAIP
GQFDLIVSNP PYIALAEMPG LSPEVRDWEP WGALTDHGDG LTAYRRIAEG AAARLAPGGR
IAVEIGYEQG PAVAALFAEA GFGHVEIRQD LGQRDRVILA HI
//
